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PR01645

Identifier
TRPCHANNEL4  [View Relations]  [View Alignment]  
Accession
PR01645
No. of Motifs
6
Creation Date
13-NOV-2001
Title
Transient receptor potential channel 4 signature
Database References
PRINTS; PR01097 TRNSRECEPTRP
PRODOM; PD041982
MIM; 603651
Literature References
1. ZHU, X., JIANG, M., PEYTON, M., BOULAY, G., HURST, R., STEFANI, E. 
AND BIRNBAUMER, L.
Trp, a novel mammalian gene family essential for agonist-activated 
capacitative Ca2+ entry.
CELL 85 661-671 (1996).
 
2. BOULAY, G., ZHU, X., PEYTON, M., JIANG, M., HURST, R., STEFANI, E. 
AND BIRNBAUMER, L.
Cloning and expression of a novel mammalian homolog of Drosophila transient
receptor potential (Trp) involved in calcium entry secondary to activation 
of receptors coupled by the Gq class of G protein.
J.BIOL.CHEM. 272 29672-29680 (1997).
 
3. CLAPHAM, D., RUNNELS, L. AND STRUBING, C.
The TRP ion channel family.
NAT.REV.NEUROSCI. 2 6387-396 (2001). 
 
4. HARTENECK, C., PLANT, T. AND SCHULTZ, G.
From worm to man: three subfamilies of TRP channels.
TRENDS NEUROSCI. 23 159-166 (2000).
 
5. PHILIPP, S., CAVALIE, A., FREICHEL, M., WISSENBACH, U., ZIMMER, S., 
TROST, C., MARQUART, A., MURAKAMI, M. AND FLOCKERZI, V.
A mammalian capacitative calcium entry channel homologous to Drosophila TRP
and TRPL.
EMBO J. 15 6166-6171 (1996).
 
6. SCHAEFER, M., PLANT, T., OBUKHOV, A., HOFMANN, T., GUDERMANN, T. AND
SCHULTZ, G.
Receptor-mediated regulation of the nonselective cation channels TRPC4 and 
TRPC5.
J.BIOL.CHEM. 275 17517-17526 (2000).

Documentation
Transient receptor potential (Trp) and related proteins are thought to be
Ca2+ ion channel subunits that mediate capacitative Ca2+ entry in response 
to a range of external and internal cell stimuli. Such Ca2+ entry is thought 
to be an essential component of cellular responses to many hormones and
growth factors, and acts to replenish intracellular Ca2+ stores that have
been emptied through the action of inositol triphosphate (IP3) and other 
agents. In non-excitable cells, i.e. those that lack voltage-gated Ca2+
channels, such as hepatocytes, this mode of Ca2+ entry is thought to be an
important step in generating the oscillations of intracellular Ca2+
concentration that characterise their response to stimulatory agents [1].
 
Studies on the visual transduction system in Drosophila led to the molecular
cloning of Trp and the cDNA of a related protein, Trp-like, which show
similarity to voltage gated Ca2+ channels in the regions known as S3 through
S6, including the S5-S6 linker that forms the ion-selective channel pore [2].
This provided evidence that Trp and/or related proteins might form mammalian
capacitative Ca2+ entry channels. 
 
A number of Trp and Trp-like channel gene isoforms have now been cloned, 
including several mammalian homologues. The Trp family is thought to encode
at least 20 Ca2+-permeable channel proteins. Hydropathy analysis suggests 
that they share a common transmembrane (TM) topology. Each family member is 
predicted to possess 6 TM domains with intracellular N- and C-termini, which
is similar to the core structure of the pore-forming subunits of the voltage
-gated Na+ and Ca2+ channels. By analogy with these proteins, which have 
4 linked domains of 6 TM segments, it is likely that Trp channels are
homo- or heterotetramers of 4 single subunits [3].
 
The Trp family can be divided on the basis of sequence similarity into 3
subfamilies: short (S), long (L) and osm-like (O) Trp channels [4]. The
STrp subfamily includes Drosophila Trp and Trpl-like, and the mammalian
homologues TrpC1-7. Channels of the STrpC subfamily are activated following
receptor-mediated stimulation of different isoforms of phospholipase C [4].
 
TrpC4 was originally cloned from bovine tissue [5]; rat, mouse and human
isoforms have also been identified. Expression studies have demonstrated 
that TrpC4 is able to form homomeric cation channels that are activated 
following stimulation of Gq-coupled receptors and by receptor tyrosine 
kinases [6].
 
TRPCHANNEL4 is a 6-element fingerprint that provides a signature for
transient receptor potential channel 4. The fingerprint was derived from an 
initial alignment of 4 sequences: the motifs were drawn from conserved 
regions in the C-terminal portion of the alignment, focusing on those 
sections that characterise TrpC4 but distinguish it from other family 
members - all motifs reside within the the cytoplasmic C-terminus. A single 
iteration on SPTR40_18f was required to reach convergence, no further 
sequences being identified beyond the starting set. 
Summary Information
4 codes involving  6 elements
0 codes involving 5 elements
0 codes involving 4 elements
0 codes involving 3 elements
0 codes involving 2 elements
Composite Feature Index
6444444
5000000
4000000
3000000
2000000
123456
True Positives
O35119        P79100        TRP4_HUMAN    TRP4_MOUSE    
Sequence Titles
O35119      TRANSIENT RECEPTOR POTENTIAL - RATTUS NORVEGICUS (RAT). 
P79100 CAPACITATIVE CALCIUM ENTRY CHANNEL 1 (CAPACITATIVE CALCIUM ENTRY CHANNEL 1, TRUNCATED VARIANT BCCE1DELTA514) - BOS TAURUS (BOVINE).
TRP4_HUMAN Short transient receptor potential channel 4 (TrpC4) (trp-related protein 4) (hTrp-4) (hTrp4) - Homo sapiens (Human).
TRP4_MOUSE Short transient receptor potential channel 4 (TrpC4) (Receptor- activated cation channel TRP4) (Capacitative calcium entry channel Trp4) - Mus musculus (Mouse).
Scan History
SPTR40_18f 1  150  NSINGLE    
Initial Motifs
Motif 1  width=12
Element Seqn Id St Int Rpt
RGSKLSTIQSAN TRP4_HUMAN 755 755 -
RGSKLSTIQSAN TRP4_MOUSE 755 755 -
RGSKLSTIQSAN O35119 755 755 -
RGSKLSTVQSAQ P79100 757 757 -

Motif 2 width=17
Element Seqn Id St Int Rpt
SADSDEKSDSEGNSKDK TRP4_HUMAN 774 7 -
SADSDEKSQSEGNGKDK TRP4_MOUSE 770 3 -
SADSDEKSHSEGNGKDK O35119 773 6 -
SADSDEKSDNEGSSKDK P79100 776 7 -

Motif 3 width=23
Element Seqn Id St Int Rpt
KNFSLFDLTTLIHPRSAAIASER TRP4_HUMAN 792 1 -
KNLSLFDLTTLIHPRSAAIASER TRP4_MOUSE 788 1 -
KNLSLFDLTTLIHPRSAVIASER O35119 791 1 -
KNFSLFDLTTLIHPRSAAIAAER P79100 794 1 -

Motif 4 width=23
Element Seqn Id St Int Rpt
ISNGSALVVQEPPREKQRKVNFV TRP4_HUMAN 817 2 -
LSNGSALVVQEPPREKQRKVNFV TRP4_MOUSE 813 2 -
LSNGSALVVQEPPREKQRKVNFV O35119 816 2 -
ISNGSALVVQEPPREKQRKVNFV P79100 819 2 -

Motif 5 width=14
Element Seqn Id St Int Rpt
DIKNFGLFHRRSKQ TRP4_HUMAN 841 1 -
DIKNFGLFHRRSKQ TRP4_MOUSE 837 1 -
DIKNFGLFHRRSKQ O35119 840 1 -
DIRHFGLFHRRSKQ P79100 843 1 -

Motif 6 width=30
Element Seqn Id St Int Rpt
SIPGLSEQCVLVDHRERNTDTLGLQVGKRV TRP4_HUMAN 898 43 -
SIPGLNEQCVLVDHRERNTDTLGLQVGKRV TRP4_MOUSE 894 43 -
SIPGLNEQCVLVDHRERNTDTLGLQVGKRV O35119 897 43 -
NIPGLSEQCILVDHRERNTDSLGVQVSKRV P79100 901 44 -
Final Motifs
Motif 1  width=12
Element Seqn Id St Int Rpt
RGSKLSTIQSAN TRP4_HUMAN 755 755 -
RGSKLSTIQSAN TRP4_MOUSE 755 755 -
RGSKLSTIQSAN O35119 755 755 -
RGSKLSTVQSAQ P79100 757 757 -

Motif 2 width=17
Element Seqn Id St Int Rpt
SADSDEKSDSEGNSKDK TRP4_HUMAN 774 7 -
SADSDEKSQSEGNGKDK TRP4_MOUSE 770 3 -
SADSDEKSHSEGNGKDK O35119 773 6 -
SADSDEKSDNEGSSKDK P79100 776 7 -

Motif 3 width=23
Element Seqn Id St Int Rpt
KNFSLFDLTTLIHPRSAAIASER TRP4_HUMAN 792 1 -
KNLSLFDLTTLIHPRSAAIASER TRP4_MOUSE 788 1 -
KNLSLFDLTTLIHPRSAVIASER O35119 791 1 -
KNFSLFDLTTLIHPRSAAIAAER P79100 794 1 -

Motif 4 width=23
Element Seqn Id St Int Rpt
ISNGSALVVQEPPREKQRKVNFV TRP4_HUMAN 817 2 -
LSNGSALVVQEPPREKQRKVNFV TRP4_MOUSE 813 2 -
LSNGSALVVQEPPREKQRKVNFV O35119 816 2 -
ISNGSALVVQEPPREKQRKVNFV P79100 819 2 -

Motif 5 width=14
Element Seqn Id St Int Rpt
DIKNFGLFHRRSKQ TRP4_HUMAN 841 1 -
DIKNFGLFHRRSKQ TRP4_MOUSE 837 1 -
DIKNFGLFHRRSKQ O35119 840 1 -
DIRHFGLFHRRSKQ P79100 843 1 -

Motif 6 width=30
Element Seqn Id St Int Rpt
SIPGLSEQCVLVDHRERNTDTLGLQVGKRV TRP4_HUMAN 898 43 -
SIPGLNEQCVLVDHRERNTDTLGLQVGKRV TRP4_MOUSE 894 43 -
SIPGLNEQCVLVDHRERNTDTLGLQVGKRV O35119 897 43 -
NIPGLSEQCILVDHRERNTDSLGVQVSKRV P79100 901 44 -